4ZXM

Crystal structure of PGRP domain from Branchiostoma belcheri tsingtauense peptidoglycan recognition protein 3

4ZXM の概要

• エントリーDOI: 10.2210/pdb4zxm/pdb
• 分子名称: PGRP domain of peptidoglycan recognition protein 3 (2 entities in total)
• 機能のキーワード: peptidoglycan recognition protein, amidase, hydrolase
• 由来する生物種: Branchiostoma belcheri tsingtauense
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27569.44

構造登録者

Wang, W.J.,Cheng, W.,Jiang, Y.L.,Yu, H.M.,Luo, M. (登録日: 2015-05-20, 公開日: 2015-10-14, 最終更新日: 2024-10-30)

主引用文献

Wang, W.J.,Cheng, W.,Luo, M.,Yan, Q.,Yu, H.M.,Li, Q.,Cao, D.D.,Huang, S.,Xu, A.,Mariuzza, R.A.,Chen, Y.,Zhou, C.Z.
Activity Augmentation of Amphioxus Peptidoglycan Recognition Protein BbtPGRP3 via Fusion with a Chitin Binding Domain
Plos One, 10:e0140953-e0140953, 2015

PubMed Abstract: Peptidoglycan recognition proteins (PGRPs), which have been identified in most animals, are pattern recognition molecules that involve antimicrobial defense. Resulting from extraordinary expansion of innate immune genes, the amphioxus encodes many PGRPs of diverse functions. For instance, three isoforms of PGRP encoded by Branchiostoma belcheri tsingtauense, termed BbtPGRP1~3, are fused with a chitin binding domain (CBD) at the N-terminus. Here we report the 2.7 Å crystal structure of BbtPGRP3, revealing an overall structure of an N-terminal hevein-like CBD followed by a catalytic PGRP domain. Activity assays combined with site-directed mutagenesis indicated that the individual PGRP domain exhibits amidase activity towards both DAP-type and Lys-type peptidoglycans (PGNs), the former of which is favored. The N-terminal CBD not only has the chitin-binding activity, but also enables BbtPGRP3 to gain a five-fold increase of amidase activity towards the Lys-type PGNs, leading to a significantly broadened substrate spectrum. Together, we propose that modular evolution via domain shuffling combined with gene horizontal transfer makes BbtPGRP1~3 novel PGRPs of augmented catalytic activity and broad recognition spectrum.

PubMed: 26479246
DOI: 10.1371/journal.pone.0140953

実験手法

X-RAY DIFFRACTION (2.8 Å)